Human Aβ-binding alcohol dehydrogenase (“ABAD,” also known as “ERAS” and “HSD-10”) was the only protein identified from four positive clones that bound Aβ protein (also referred to as “Aβ”) in a yeast two-hybrid screen against human brain and HeLa cDNA libraries (1, 2). Biochemical characterization has established that the interaction between ABAD and Aβ is highly specific and starts to occur at nanomolar concentrations. At micromolar concentrations, Aβ, likely in its oligomeric form, inhibits ABAD enzymatic activity (1, 3, 4). ABAD appears to have an essential physiological role in mitochondria (1, 3), and mutational inactivation of Drosophilia ABAD (scully) resulted in a lethal phenotype (5). ABAD is up-regulated in affected neurons in AD (1) (FIG. 5) and co-expression of ABAD with mutant amyloid precursor protein (mAPP) exacerbates Aβ-induced cellular oxidant stress and cell death (1, 3).